{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,30]],"date-time":"2026-09-30T18:58:55Z","timestamp":1790794735296,"version":"4.1.0"},"reference-count":46,"publisher":"American Physiological Society","issue":"4","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["American Journal of Physiology-Cell Physiology"],"published-print":{"date-parts":[[2002,10,1]]},"abstract":"<jats:p> A countertransport of H<jats:sup>+<\/jats:sup> is coupled to Ca<jats:sup>2+<\/jats:sup> transport across the sarcoplasmic reticulum (SR) membrane. We propose that SR carbonic anhydrase (CA) accelerates the CO<jats:sub>2<\/jats:sub>-HCO[Formula: see text]reaction so that H<jats:sup>+<\/jats:sup> ions, which are exchanged for Ca<jats:sup>2+<\/jats:sup> ions, are produced or buffered in the SR at sufficient rates. Inhibition of this SR-CA is expected to reduce the rate of H<jats:sup>+<\/jats:sup> fluxes, which then will retard the kinetics of Ca<jats:sup>2+<\/jats:sup> transport. Fura 2 signals and isometric force were simultaneously recorded in fiber bundles of the soleus (SOL) and extensor digitorum longus (EDL) from rats in the absence and presence of the lipophilic CA inhibitors L-645151, chlorzolamide (CLZ), and ethoxzolamide (ETZ), as well as the hydrophilic inhibitor acetazolamide (ACTZ). Fura 2 and force signals were analyzed for time to peak (TTP), 50% decay time ( t <jats:sub>50<\/jats:sub>), and their amplitudes. L-645151, CLZ, and ETZ significantly increased TTP of fura 2 by 10\u201325 ms in SOL and by 5\u20137 ms in EDL and TTP of force by 6\u201330 ms in both muscles. L-645151 and ETZ significantly prolonged t <jats:sub>50<\/jats:sub> of fura 2 and force by 20\u201355 and 40\u2013160 ms, respectively, in SOL and EDL. L-645151, CLZ, and ETZ also increased peak force of single twitches and amplitudes of fura fluorescence ratio (R<jats:sub>340\/380<\/jats:sub>) at an excitation wavelength of 340 to 380 nm. All effects of CA inhibitors on fura 2 and force signals could be reversed. ACTZ did not affect TTP, t <jats:sub>50<\/jats:sub>, and amplitudes of fura 2 signals or force. L-645151, CLZ, and ETZ had no effects on myosin-, Ca<jats:sup>2+<\/jats:sup>-, and Na<jats:sup>+<\/jats:sup>-K<jats:sup>+<\/jats:sup>-ATPase activities, nor did they affect the amplitude and half-width of action potentials. We conclude that inhibition of SR-CA by impairing H<jats:sup>+<\/jats:sup> countertransport is responsible for deceleration of intracellular Ca<jats:sup>2+<\/jats:sup>transients and contraction times. <\/jats:p>","DOI":"10.1152\/ajpcell.00106.2002","type":"journal-article","created":{"date-parts":[[2013,5,14]],"date-time":"2013-05-14T00:10:48Z","timestamp":1368490248000},"page":"C1242-C1253","source":"Crossref","is-referenced-by-count":20,"title":["Inhibition of muscle carbonic anhydrase slows the Ca<sup>2+<\/sup>  transient in rat skeletal muscle fibers"],"prefix":"10.1152","volume":"283","author":[{"given":"Petra","family":"Wetzel","sequence":"first","affiliation":[{"name":"Zentrum Physiologie, Medizinische Hochschule Hannover, 30623 Hannover, Germany"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Tanja","family":"Kleinke","sequence":"additional","affiliation":[{"name":"Zentrum Physiologie, Medizinische Hochschule Hannover, 30623 Hannover, 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